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CYCP_RHOTE
ID   CYCP_RHOTE              Reviewed;         133 AA.
AC   P00153;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   03-AUG-2022, entry version 81.
DE   RecName: Full=Cytochrome c';
OS   Rhodocyclus tenuis (Rhodospirillum tenue).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Rhodocyclales;
OC   Rhodocyclaceae; Rhodocyclus.
OX   NCBI_TaxID=1066;
RN   [1]
RP   PROTEIN SEQUENCE.
RX   PubMed=221823; DOI=10.1038/278661a0;
RA   Ambler R.P., Meyer T.E., Kamen M.D.;
RT   "Anomalies in amino acid sequences of small cytochromes c and cytochromes
RT   c' from two species of purple photosynthetic bacteria.";
RL   Nature 278:661-662(1979).
CC   -!- FUNCTION: Cytochrome c' is the most widely occurring bacterial c-type
CC       cytochrome. Cytochromes c' are high-spin proteins and the heme has no
CC       sixth ligand. Their exact function is not known.
CC   -!- PTM: Binds 1 heme group per subunit.
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DR   PIR; A00146; CCQFCT.
DR   AlphaFoldDB; P00153; -.
DR   SMR; P00153; -.
DR   GO; GO:0042597; C:periplasmic space; IEA:InterPro.
DR   GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   InterPro; IPR010980; Cyt_c/b562.
DR   InterPro; IPR002321; Cyt_c_II.
DR   InterPro; IPR012127; Cyt_c_prime.
DR   InterPro; IPR015984; Cyt_c_prime_subgr.
DR   Pfam; PF01322; Cytochrom_C_2; 1.
DR   PIRSF; PIRSF000027; Cytc_c_prime; 1.
DR   PRINTS; PR00608; CYTCHROMECII.
DR   SUPFAM; SSF47175; SSF47175; 1.
DR   PROSITE; PS51009; CYTCII; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Electron transport; Heme; Iron; Metal-binding;
KW   Transport.
FT   CHAIN           1..133
FT                   /note="Cytochrome c'"
FT                   /id="PRO_0000108378"
FT   BINDING         122
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /note="covalent"
FT                   /evidence="ECO:0000269|PubMed:221823"
FT   BINDING         125
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /note="covalent"
FT                   /evidence="ECO:0000269|PubMed:221823"
FT   BINDING         126
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
SQ   SEQUENCE   133 AA;  14313 MW;  76EE532B580C2838 CRC64;
     EPAKSEDLIK WRQSAYQVLH WNMDRLKANI DSPQYNKDDG IKAANTIAAI ANSGMGSLFA
     AGTETGKGWH PTSVKPAFFT DGKKVGEVAV AFNKEANELA KVAATGDAAA VKAQFGKVGQ
     TCKACHDDFR RKD
 
 
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